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Crystallization of recombinant Crithidia fasciculata tryparedoxin.
Alphey, M S; Tetaud, E; Gourley, D G; Fairlamb, A H; Hunter, W N.
Afiliação
  • Alphey MS; Department of Biochemistry, University of Dundee, Dundee, DD1 5EH, United Kingdom.
J Struct Biol ; 126(1): 76-9, 1999 Jun 01.
Article em En | MEDLINE | ID: mdl-10329491
Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51. 47, and c = 73.41 A, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-A resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.
Assuntos
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Base de dados: MEDLINE Assunto principal: Tiorredoxinas / Proteínas de Protozoários Limite: Animals Idioma: En Revista: J Struct Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 1999 Tipo de documento: Article País de afiliação: Reino Unido
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Base de dados: MEDLINE Assunto principal: Tiorredoxinas / Proteínas de Protozoários Limite: Animals Idioma: En Revista: J Struct Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 1999 Tipo de documento: Article País de afiliação: Reino Unido